RGT1_YEAST - dbPTM
RGT1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RGT1_YEAST
UniProt AC P32862
Protein Name Glucose transport transcription regulator RGT1
Gene Name RGT1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1170
Subcellular Localization Nucleus . Cytoplasm .
Protein Description Glucose-responsive transcription factor that regulates expression of several glucose transporter (HXT) genes in response to glucose. In the absence of glucose, it functions as a transcriptional repressor, whereas high concentrations of glucose cause it to function as a transcriptional activator. In cells growing on low levels of glucose, has a neutral role, neither repressing nor activating transcription. Binds the consensus binding site sequence 5'-CGGANNA-3', of which multiple copies are present in all HXT promoters regulated by RGT1..
Protein Sequence MNELNTVSTNSSDSTKNGGTSNSPDDMDSAAAASHAIKKRTKASRACDQCRKKKIKCDYKDEKGVCSNCQRNGDRCSFDRVPLKRGPSKGYTRSTSHPRTNEIQDHNNSRSYNTFDNSNNTLNNNTGNSGDNGINSNTVPSTPSRSNSVLLPPLTQYIPQAGGIPPSFQNPAIQSTMPAGNIGQQQFWKVPYHEFQHQRKGSIDSLQSDISVRTLNPNEQLSYNTVQQSPITNKHTNDSGNANGSVTGSGSASGSGGYWSFIRTSGLLAPTDDHNGEQTRRSSSIPSLLRNTSNSLLLGGQPQLPPPQQQSQPQAHQQKLQQGQNLYSYSQFSQQQPYNPSISSFGQFAANGFHSRQGSVASEAMSPSAPAMFTSTSTNPVNVAQQTQRPQGQQVPQFSSELDGNKRRQSAPVSVTLSTDRLNGNENNNGEINNNNGSNNSGSSKDTSQHSQESVTTPAALEASSPGSTPQRSTKKRRKSYVSKKTKPKRDSSISITSKDSAHPMTTSSTIAYGQISDVDLIDTYYEFIHVGFPIIPLNKTTLTSDLLLVNTQPISNIHEVNSYVILWFRNSLELLVRVALKQKPGGKFFDNIVGVALSPSNDNNKAGFTTATARDDAEKTRRDSHNEVQDTLEVQSVFIAALNECFQKIVDIHPKFRENNDQISPKIKVIYLSTFILLNYILAFVGYDNSFVLGMSVTIFNEFKLYKLLLFPEPDINDVKPPVDEEVSTGNGNTKTSEFEIGSESAGHMNPSNSPNSMDENISHYSVLFKRLYVLLSVFDSLQSCAFGGPKLLNISIQGSTERFFSNDLGSKWCLEQSQLRLKSVLQSLKLGELMSELTRNRISMNGNRKPGFDITNSSSLLSEYVETQPLSVAQLFCKLLIGKHNFINCLLSLYDSEAGVYSDLTLDLSSKIADSLCSLISIILQVLTLILRLNPTNSIDFNYRPPNPPANNPTVQEGPSAMGSSPVAGNLSAAPPSEGNPDFYKKLLGLKQDTGTILSDLCRGIISPFAIAILHEVYNITELVKQMPTSLISIMMTATTTQNTQDTKKSQDLVMKLSNSMNEVVQITSVLTMIKPFKIFEHELNKPIMSLTGGLSSTTRNDVMWPKSGQGLRESSVMKTLLDERRTSGTQPTTAPVAAEEPRLENVALENFVSIGWKLLDDSELGWY
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
20PhosphorylationDSTKNGGTSNSPDDM
CCCCCCCCCCCHHHH		26.5722369663
21PhosphorylationSTKNGGTSNSPDDMD
CCCCCCCCCCHHHHH		38.2922369663
23PhosphorylationKNGGTSNSPDDMDSA
CCCCCCCCHHHHHHH		29.4922369663
29PhosphorylationNSPDDMDSAAAASHA
CCHHHHHHHHHHHHH		17.1120377248
41PhosphorylationSHAIKKRTKASRACD
HHHHHHHHHHHHHHH		39.5828889911
94PhosphorylationPSKGYTRSTSHPRTN
CCCCCCCCCCCCCCC		26.8522369663
95PhosphorylationSKGYTRSTSHPRTNE
CCCCCCCCCCCCCCC		27.9722369663
96PhosphorylationKGYTRSTSHPRTNEI
CCCCCCCCCCCCCCC		32.5122369663
100PhosphorylationRSTSHPRTNEIQDHN
CCCCCCCCCCCCCCC		41.4722369663
109PhosphorylationEIQDHNNSRSYNTFD
CCCCCCCCCCCCCCC		28.1127214570
141PhosphorylationINSNTVPSTPSRSNS
CCCCCCCCCCCCCCC		48.9223749301
144PhosphorylationNTVPSTPSRSNSVLL
CCCCCCCCCCCCCCC		48.7219779198
146PhosphorylationVPSTPSRSNSVLLPP
CCCCCCCCCCCCCCC		37.4828889911
202PhosphorylationFQHQRKGSIDSLQSD
CHHHCCCCHHHHCCC		26.6822369663
205PhosphorylationQRKGSIDSLQSDISV
HCCCCHHHHCCCCEE		27.0022369663
208PhosphorylationGSIDSLQSDISVRTL
CCHHHHCCCCEEEEC		42.0522369663
214PhosphorylationQSDISVRTLNPNEQL
CCCCEEEECCCCCCC		28.8225704821
229PhosphorylationSYNTVQQSPITNKHT
CCCCCCCCCCCCCCC		10.9421082442
232PhosphorylationTVQQSPITNKHTNDS
CCCCCCCCCCCCCCC		41.4128889911
245PhosphorylationDSGNANGSVTGSGSA
CCCCCCCCEEECCCC		19.1319779198
247PhosphorylationGNANGSVTGSGSASG
CCCCCCEEECCCCCC		27.5928889911
249PhosphorylationANGSVTGSGSASGSG
CCCCEEECCCCCCCC		21.8719779198
251PhosphorylationGSVTGSGSASGSGGY
CCEEECCCCCCCCCC		22.4328889911
279PhosphorylationDDHNGEQTRRSSSIP
CCCCCCCCCCHHCHH		24.6128889911
282PhosphorylationNGEQTRRSSSIPSLL
CCCCCCCHHCHHHHH		25.7528889911
283PhosphorylationGEQTRRSSSIPSLLR
CCCCCCHHCHHHHHH		30.4023749301
284PhosphorylationEQTRRSSSIPSLLRN
CCCCCHHCHHHHHHC		39.5015665377
287PhosphorylationRRSSSIPSLLRNTSN
CCHHCHHHHHHCCCC		38.0623749301
292PhosphorylationIPSLLRNTSNSLLLG
HHHHHHCCCCCEECC		23.8919779198
295PhosphorylationLLRNTSNSLLLGGQP
HHHCCCCCEECCCCC		21.8419779198
344PhosphorylationPYNPSISSFGQFAAN
CCCCCHHHHHHHHHC		31.5519779198
410PhosphorylationDGNKRRQSAPVSVTL
CCCCCCCCCCEEEEE		32.5017330950
414PhosphorylationRRQSAPVSVTLSTDR
CCCCCCEEEEEECCC		14.3423749301
416PhosphorylationQSAPVSVTLSTDRLN
CCCCEEEEEECCCCC		13.9027017623
418PhosphorylationAPVSVTLSTDRLNGN
CCEEEEEECCCCCCC		20.9219779198
419PhosphorylationPVSVTLSTDRLNGNE
CEEEEEECCCCCCCC		28.4019779198
447PhosphorylationNSGSSKDTSQHSQES
CCCCCCCCCHHHHHC		33.7429136822
448PhosphorylationSGSSKDTSQHSQESV
CCCCCCCCHHHHHCC		35.7129136822
451PhosphorylationSKDTSQHSQESVTTP
CCCCCHHHHHCCCCH		28.1829136822
454PhosphorylationTSQHSQESVTTPAAL
CCHHHHHCCCCHHHH		19.6829136822
456PhosphorylationQHSQESVTTPAALEA
HHHHHCCCCHHHHHH		36.0229136822
457PhosphorylationHSQESVTTPAALEAS
HHHHCCCCHHHHHHC		14.5829136822
464PhosphorylationTPAALEASSPGSTPQ
CHHHHHHCCCCCCCC		27.9119779198
465PhosphorylationPAALEASSPGSTPQR
HHHHHHCCCCCCCCC		40.0929136822
468PhosphorylationLEASSPGSTPQRSTK
HHHCCCCCCCCCCCH		40.0527017623
469PhosphorylationEASSPGSTPQRSTKK
HHCCCCCCCCCCCHH		29.3829136822
486PhosphorylationKSYVSKKTKPKRDSS
HHHCCCCCCCCCCCC		57.2124961812
492PhosphorylationKTKPKRDSSISITSK
CCCCCCCCCCEEECC		33.3422369663
493PhosphorylationTKPKRDSSISITSKD
CCCCCCCCCEEECCC		25.3322369663
495PhosphorylationPKRDSSISITSKDSA
CCCCCCCEEECCCCC		23.0522369663
497PhosphorylationRDSSISITSKDSAHP
CCCCCEEECCCCCCC		23.9624961812
498PhosphorylationDSSISITSKDSAHPM
CCCCEEECCCCCCCC		32.5624961812
599PhosphorylationNIVGVALSPSNDNNK
CEEEEEECCCCCCCC		19.2825521595
601PhosphorylationVGVALSPSNDNNKAG
EEEEECCCCCCCCCC		54.1421440633
744PhosphorylationTSEFEIGSESAGHMN
CEEEEECCCCCCCCC		33.7624961812
746PhosphorylationEFEIGSESAGHMNPS
EEEECCCCCCCCCCC		41.0521551504
753PhosphorylationSAGHMNPSNSPNSMD
CCCCCCCCCCCCCCC		44.9624961812
755PhosphorylationGHMNPSNSPNSMDEN
CCCCCCCCCCCCCCC		29.7828889911
758PhosphorylationNPSNSPNSMDENISH
CCCCCCCCCCCCCHH		30.8728889911
764PhosphorylationNSMDENISHYSVLFK
CCCCCCCHHHHHHHH		28.1428889911
819PhosphorylationSKWCLEQSQLRLKSV
CCHHHHHHHHHHHHH		23.0830377154
1031PhosphorylationELVKQMPTSLISIMM
HHHHHCCHHHHHHHH		30.7227017623
1032PhosphorylationLVKQMPTSLISIMMT
HHHHCCHHHHHHHHH		20.1727017623
1035PhosphorylationQMPTSLISIMMTATT
HCCHHHHHHHHHEEC		15.1027017623
1046PhosphorylationTATTTQNTQDTKKSQ
HEECCCCCCCCHHHH		20.2927017623
1129PhosphorylationTLLDERRTSGTQPTT
HHHHHHHCCCCCCCC		37.4217563356
1130PhosphorylationLLDERRTSGTQPTTA
HHHHHHCCCCCCCCC		37.7217330950
1132PhosphorylationDERRTSGTQPTTAPV
HHHHCCCCCCCCCCC		31.0121082442
1135PhosphorylationRTSGTQPTTAPVAAE
HCCCCCCCCCCCCCC		26.2721440633
1136PhosphorylationTSGTQPTTAPVAAEE
CCCCCCCCCCCCCCC		35.3329688323
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of RGT1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RGT1_YEAST !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of RGT1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MTH1_YEASTMTH1physical
14508605
STD1_YEASTSTD1physical
14508605
CYC8_YEASTCYC8physical
15489524
STD1_YEASTSTD1physical
15489524
MTH1_YEASTMTH1physical
15489524
RGT1_YEASTRGT1physical
15489524
GRR1_YEASTGRR1genetic
11576534
SNF3_YEASTSNF3genetic
11576534
SKO1_YEASTSKO1genetic
15014083
HXKB_YEASTHXK2physical
16528100
MED8_YEASTMED8physical
16528100
MGA2_YEASTMGA2genetic
19547744
VPS72_YEASTVPS72genetic
20959818
SSN2_YEASTSSN2genetic
20959818
HCM1_YEASTHCM1genetic
20959818
RPI1_YEASTRPI1genetic
20959818
MGA2_YEASTMGA2genetic
20959818
ASG1_YEASTASG1genetic
20959818
CUP2_YEASTCUP2genetic
20959818
PFD5_YEASTGIM5genetic
20959818
SNF1_YEASTSNF1genetic
21127252
MTH1_YEASTMTH1genetic
23234240
HXT2_YEASTHXT2genetic
23234240
MTH1_YEASTMTH1physical
23468525
CYC8_YEASTCYC8physical
23468525
PP2C1_YEASTPTC1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
HAP3_YEASTHAP3genetic
27708008
GPR1_YEASTGPR1genetic
27708008
TMN2_YEASTTMN2genetic
27708008
ODO2_YEASTKGD2genetic
27708008
DHAS_YEASTHOM2genetic
27708008
IPK1_YEASTIPK1genetic
27708008
YPS7_YEASTYPS7genetic
27708008
BCS1_YEASTBCS1genetic
27708008
RLA4_YEASTRPP2Bgenetic
27708008
SNF1_YEASTSNF1genetic
27708008
SNF6_YEASTSNF6genetic
27708008
DAL81_YEASTDAL81genetic
27708008
BUL2_YEASTBUL2genetic
27708008
PET8_YEASTPET8genetic
27708008
EAF7_YEASTEAF7genetic
27708008
VPS21_YEASTVPS21genetic
27708008
TBCA_YEASTRBL2genetic
27708008
VPS4_YEASTVPS4genetic
27708008
CSG2_YEASTCSG2genetic
29674565
PAT1_YEASTPAT1genetic
29674565
PBS2_YEASTPBS2genetic
29674565
INO2_YEASTINO2genetic
29674565
AMPD_YEASTAMD1genetic
29674565
FUMH_YEASTFUM1genetic
29674565
UME6_YEASTUME6genetic
29674565
SPT3_YEASTSPT3genetic
29674565
VTI1_YEASTVTI1genetic
29674565
COG6_YEASTCOG6genetic
29674565
PRA1_YEASTYIP3genetic
29674565
COPZ_YEASTRET3genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RGT1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-229; THR-232;SER-284; SER-410; SER-493; SER-599; SER-601; THR-1129; SER-1130;THR-1132 AND THR-1135, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1129; SER-1130 ANDTHR-1132, AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202; SER-229 ANDSER-284, AND MASS SPECTROMETRY.

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